ADP‐ribosylation of histone variant H2AX promotes base excision repair-Reference-Cited by-同舟云学术

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ADP‐ribosylation of histone variant H2AX promotes base excision repair

Published:2020-12-02 Issue:2 Volume:40 Page:
ISSN:0261-4189
Container-title:The EMBO Journal
language:en
Short-container-title:The EMBO Journal

Author:

Chen Qian¹^ORCID,Bian Chunjing¹,Wang Xin¹,Liu Xiuhua¹,Ahmad Kassab Muzaffer¹,Yu Yonghao²,Yu Xiaochun¹^ORCID

Affiliation:

1. Department of Cancer Genetics and Epigenetics Beckman Research Institute City of Hope Medical Center Duarte CA USA

2. Department of Biochemistry University of Texas Southwestern Medical Center Dallas TX USA

Funder

Pancreatic Cancer Action Network

Tower Cancer Research Foundation

National Institutes of Health

Welch Foundation

Publisher

EMBO

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Link

https://onlinelibrary.wiley.com/doi/pdf/10.15252/embj.2020104542

Reference81 articles.

1. Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites

2. Expression of phosphorylated histone H2AX as a surrogate of cell killing by drugs that create DNA double‐strand breaks;Banath JP;Cancer Res,2003

3. Chromatin remodeling in DNA double-strand break repair

4. New Quantitative Mass Spectrometry Approaches Reveal Different ADP-ribosylation Phases Dependent On the Levels of Oxidative Stress

5. Active-Site Mutations of Diphtheria Toxin: Role of Tyrosine-65 in NAD Binding and ADP-Ribosylation

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